ID A0A4V4NDV2_9PEZI Unreviewed; 476 AA.
AC A0A4V4NDV2;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=mitochondrial processing peptidase {ECO:0000256|ARBA:ARBA00012299};
DE EC=3.4.24.64 {ECO:0000256|ARBA:ARBA00012299};
DE AltName: Full=Beta-MPP {ECO:0000256|ARBA:ARBA00031018};
GN ORFNames=CH35J_001332 {ECO:0000313|EMBL:TID06252.1};
OS Colletotrichum higginsianum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=80884 {ECO:0000313|EMBL:TID06252.1, ECO:0000313|Proteomes:UP000305883};
RN [1] {ECO:0000313|EMBL:TID06252.1, ECO:0000313|Proteomes:UP000305883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF305635-RFP {ECO:0000313|EMBL:TID06252.1,
RC ECO:0000313|Proteomes:UP000305883};
RX PubMed=31028389; DOI=.1093/gbe/evz087;
RA Tsushima A., Gan P., Kumakura N., Narusaka M., Takano Y., Narusaka Y.,
RA Shirasu K.;
RT "Genomic Plasticity Mediated by Transposable Elements in the Plant
RT Pathogenic Fungus Colletotrichum higginsianum.";
RL Genome Biol. Evol. 11:1487-1500(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal transit peptides from precursor proteins
CC imported into the mitochondrion, typically with Arg in position P2.;
CC EC=3.4.24.64; Evidence={ECO:0000256|ARBA:ARBA00001098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|RuleBase:RU004447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TID06252.1}.
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DR EMBL; MWPZ01000001; TID06252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V4NDV2; -.
DR EnsemblFungi; CCF40855; CCF40855; CH063_00368.
DR Proteomes; UP000305883; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000305883};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 52..198
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 204..392
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 476 AA; 52860 MW; AB91E1883FF38113 CRC64;
MASRRLALNL SQGLRSRAAL SRASPITRGF ATPSNSPFGK TQTTTLKNGL TVATDYSPFA
QTSTVGVWID AGSRAETDET NGTAHFLEHL AFKGTTNRTQ QQLELEIENM GGHLNAYTSR
ENTVYFAKAF NSDVPQTVDI LADILQNSKL EESAIERERD VILRESEEVE KQMEEVVFDH
LHATAFQHQP LGRTILGPRE NIRDITRTEL TNYIKNNYTA DRMVLVGAGG IPHEKLVELA
EKNFSGLPTT GPNTQAYQLS KQKADFIGSD VRVRDDNIPT ANIAIAVEGV SWNDDDYYTA
LVAQAIVGNY DKAIGNAPHQ GSKLSGFVHK HDIANSFMSF STSYSDTGLW GIYLVTDKHD
RIDDLVYFAQ REWMRLSRNV SEAETERAKA QLKASILLSL DGTTAIAEDI GRQLITTGRR
ANPAEIERTI DAITEKDVMD FASRKLWDQD IAISAVGSIE GLFDYSRLRA TMKPKY
//
